Cellular crosstalk between TNF-α, NADPH oxidase, PKCβ2, and C2GNT in human leukocytes

Cell Signal. 2012 Apr;24(4):873-8. doi: 10.1016/j.cellsig.2011.12.003. Epub 2011 Dec 13.

Abstract

Increasing evidence suggests that chronic, sub-clinical inflammation plays an important role in the pathogenesis of diabetic retinopathy. We have established the potential role of the inflammatory enzyme, core 2 β-1, 6-N-acetylglucosaminyltransferase (C2GNT) in diabetic retinopathy. The present study was designed to explore the NADPH oxidase signaling pathway in the tumor necrosis factor-alpha (TNF-α)-induced activity of C2GNT in leukocytes. Human leukocytes (U937 cells) and an Epstein-Barr-transformed lymphoblastoid cell line deficient in p47phox (F10007 cells) were used for the study. Cells were exposed to TNF-α for 24h in the presence and absence of 1) NADPH oxidase inhibitors (apocynin and scrambled and unscrambled gp91ds-tat), 2) LY379196 (specific protein kinase C β1/2 (PKCβ1/2) inhibitor), and 3) the antioxidant tiron. Subsequent C2GNT and NADPH activity was measured and the adhesion of U937 and F10007 cells to endothelial cells was assessed. TNF-α-induced C2GNT activity (1813±326 pmol/h/mg protein) (mean±SEM) in human leukocytes was significantly reversed with apocynin (153±82 pmol/h/mg protein), unscrambled gp91ds-tat (244±122 pmol/h/mg protein) and tiron (756±87 pmol/h/mg protein). We further supported this C2GNT-NADPH oxidase link using p47phox-deficient leukocytes. The deficiency in p47phox prevented TNF-α-induced NADPH oxidase and C2GNT activity and adherence to endothelial cells. The response to TNF-α was restored by transfection with an expression plasmid containing a p47phox cDNA inserted in the sense direction. Our results demonstrate for the first time a novel signaling crosstalk between TNF-α, NADPH oxidase, PKCβ1/2 and C2GNT in leukocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetophenones / pharmacology
  • Cell Adhesion / drug effects
  • Cell Communication / drug effects
  • Cell Line, Transformed
  • Cells, Cultured
  • Endothelial Cells / cytology
  • Endothelial Cells / metabolism
  • Enzyme Inhibitors / pharmacology
  • Gene Expression Regulation
  • Genetic Complementation Test
  • Glycoproteins / pharmacology
  • Humans
  • Leukocytes / cytology
  • Leukocytes / drug effects
  • Leukocytes / metabolism*
  • N-Acetylglucosaminyltransferases / genetics
  • N-Acetylglucosaminyltransferases / metabolism*
  • NADPH Oxidases / antagonists & inhibitors
  • NADPH Oxidases / deficiency
  • NADPH Oxidases / genetics*
  • Oxidation-Reduction
  • Plasmids
  • Protein Kinase C / genetics
  • Protein Kinase C / metabolism*
  • Protein Kinase C beta
  • Signal Transduction / genetics*
  • Transfection
  • Tumor Necrosis Factor-alpha / pharmacology*

Substances

  • Acetophenones
  • Enzyme Inhibitors
  • Glycoproteins
  • Tumor Necrosis Factor-alpha
  • gp91ds-tat protein, chimeric
  • acetovanillone
  • NADPH Oxidases
  • N-Acetylglucosaminyltransferases
  • beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-acetylglucosaminyl transferase
  • Protein Kinase C
  • Protein Kinase C beta